FK506-binding protein 4 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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Q06205 (FKBP4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
FK506-binding protein 4
EC=5.2.1.8

Alternative name(s):
Peptidyl-prolyl cis-trans isomerase
Short name=PPIase
Rotamase

Gene names

Name:	FPR4
Ordered Locus Names:	YLR449W
ORF Names:	L9324.3

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	392 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Interacts with NOP53. Ref.5
Subcellular location	Nucleus Potential.
Miscellaneous	Present with 14100 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily. Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
Cellular component	Nucleus
Molecular function	Isomerase Rotamase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin silencing at rDNA Inferred from mutant phenotype. Source: SGD histone peptidyl-prolyl isomerization Inferred from direct assay. Source: SGD negative regulation of histone H3-K36 methylation Inferred from mutant phenotype. Source: SGD nucleosome assembly Inferred from direct assay. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: SGD protein folding Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from Biological aspect of Ancestor. Source: RefGenome nucleolus Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	FK506 binding Inferred from Biological aspect of Ancestor. Source: RefGenome histone binding Inferred from direct assay. Source: SGD peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HHF1	P02309	5	EBI-6956,EBI-8113
HHT1	P61830	5	EBI-6956,EBI-8098

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 392

392

FK506-binding protein 4

PRO_0000075314

Regions

Domain

306 – 392

PPIase FKBP-type

Compositional bias

191 – 199

Poly-Glu

Amino acid modifications

Modified residue

Phosphothreonine Ref.8

Modified residue

Phosphoserine Ref.3 Ref.6 Ref.7 Ref.8

Modified residue

Phosphoserine Ref.3 Ref.6 Ref.7 Ref.8

Modified residue

218

Phosphoserine Ref.8

Sequences

Sequence

Length

Mass (Da)

Tools

Q06205 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CF90C6714F04572E
Show »

FASTA

392

43,903

        10         20         30         40         50         60 
MSDMLPLATY SLNVEPYSPT PALNFKIPVT IRITMAAIDP EPFDDDKKPS TLRIIKRNPE 

        70         80         90        100        110        120 
LTRGEYYNQD NNDGLEEDES ESEQEADVPK RSVKSKKGKA VEQSESEDSE DENEIDDEFE 

       130        140        150        160        170        180 
ECVLLTLSPK GQYQQALDIT IAPEEDVQFV VTGSYTISLT GNYVKHPFDN SSDSDEDEED 

       190        200        210        220        230        240 
YYSDEESSNG EEEEEEEEED DEELSSGDDD LDDLVDASDI ESRLDELVKK DEKKKNNKKD 

       250        260        270        280        290        300 
SKRKHEEDEE ESAKPAEKKQ TTKKDKKAEK VKDSEESKPK PKTKLLEGGI IIEDRVTGKG 

       310        320        330        340        350        360 
PHAKKGTRVG MRYVGKLKNG KVFDKNTKGK PFVFKLGQGE VIKGWDIGVA GMAVGGERRI 

       370        380        390 
VIPAPYAYGK QALPGIPANS ELTFDVKLVS MK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, MASS SPECTROMETRY. Strain: 2124.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"Nop53p is a novel nucleolar 60S ribosomal subunit biogenesis protein." Sydorskyy Y., Dilworth D.J., Halloran B., Yi E.C., Makhnevych T., Wozniak R.W., Aitchison J.D. Biochem. J. 388:819-826(2005) [PubMed: 15686447] [Abstract] Cited for: INTERACTION WITH NOP53, MASS SPECTROMETRY.
[6]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, MASS SPECTROMETRY. Strain: ADR376.
[7]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, MASS SPECTROMETRY.
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-80; SER-82 AND SER-218, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U22382 Genomic DNA. Translation: AAB67528.1. BK006945 Genomic DNA. Translation: DAA09749.1.
PIR	S55971.
RefSeq	NP_013554.1. NM_001182337.1.
3D structure databases
ProteinModelPortal	Q06205.
SMR	Q06205. Positions 283-391.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-909N.
IntAct	Q06205. 62 interactions.
MINT	MINT-477847.
STRING	Q06205.
Proteomic databases
PeptideAtlas	Q06205.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR449W; YLR449W; YLR449W.
GeneID	851170.
KEGG	sce:YLR449W.
NMPDR	fig\|4932.3.peg.4585.
Organism-specific databases
CYGD	YLR449w.
SGD	S000004441. FPR4.
Phylogenomic databases
eggNOG	fuNOG10111.
GeneTree	EFGT00050000000955.
HOGENOM	HBG396046.
OMA	DITIAPE.
OrthoDB	EOG4VT96G.
Gene expression databases
ArrayExpress	Q06205.
Genevestigator	Q06205.
GermOnline	YLR449W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR023566. PPIase_FKBP. IPR001179. PPIase_FKBP_dom. [Graphical view]
KO	K14826.
PANTHER	PTHR10516. PPIase_FKBP. 1 hit.
Pfam	PF00254. FKBP_C. 1 hit. [Graphical view]
PROSITE	PS50059. FKBP_PPIASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967978.

Entry information

Entry name

FKBP4_YEAST

Accession

Primary (citable) accession number: Q06205
Secondary accession number(s): D6VZ83

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents